Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q87F36

Entry ID Method Resolution Chain Position Source
AF-Q87F36-F1 Predicted AlphaFoldDB

No variants for Q87F36

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q87F36

No associated diseases with Q87F36

5 regional properties for Q87F36

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 43 - 54 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 17 - 662 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 718 - 868 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 930 - 994 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 661 - 806 IPR033705

Functions

Description
EC Number 6.1.1.9 Ligases forming aminoacyl-tRNA and related compounds
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

3 GO annotations of molecular function

Name Definition
aminoacyl-tRNA editing activity The hydrolysis of an incorrectly aminoacylated tRNA.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
valine-tRNA ligase activity Catalysis of the reaction: L-valine + ATP + tRNA(Val) = L-valyl-tRNA(Val) + AMP + diphosphate + 2 H(+).

1 GO annotations of biological process

Name Definition
valyl-tRNA aminoacylation The process of coupling valine to valyl-tRNA, catalyzed by valyl-tRNA synthetase. The valyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a valine-accetping tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSQFTSSYDP TSFEARLYAE WEAAGHFKPS GVGQPYTILL PPPNVTGTLH MGHAFQQTLM
70 80 90 100 110 120
DALVRYHRMC GDDTLWQVGT DHAGIATEMV VSRNMALEGR GETRDSLGRE GFINKVWEWK
130 140 150 160 170 180
QQSGDTIERQ MRRLGVSADW SRSTFTMDAQ PSAAVTEAFV RWYEEGLIYR GQRLVNWDPV
190 200 210 220 230 240
LKTAISDLEV ENVQEEGMLW SIRYPLSDGV TYEHIEHDAA GNETLRETRD SLIVATTRPE
250 260 270 280 290 300
TLLGDTAVMV HPEDRRYTAL IGKTVTLPLT GRQIEVISDT YVEPTFGTGV VKVTPAHDFN
310 320 330 340 350 360
DYQVGLRHRL PMIQVLDDAA CIVSKTSIQS GIASGATSDT TDTPSDSDAS NASNQHDTLI
370 380 390 400 410 420
MPAHLAGLDR YEARKQILAD LDAQGLLVAA TPHTLQVPRG DRTGQVIEPY LTAQWFVRME
430 440 450 460 470 480
TLAARGLELV ERGAVRFVPP NWINTYRHWM ENIQDWCISR QLWWGHRIPA WFDTQGCVYV
490 500 510 520 530 540
GRSEAEVRAK HALGPEVTLT QDNDVLETWF SSQLWPFSTL GWPDPMAMAE RGFERYLPSS
550 560 570 580 590 600
VLVTGFDIIF FWVARMIMAT DHFTGNVPFH DVYITGLIRD AQGQKMSKSK GNVLDPLDII
610 620 630 640 650 660
DGITLDDLVA KRTTGLMQPK LAEKIAKATR KEFPDGIAPH GADALRFTIA ALATHGRDIK
670 680 690 700 710 720
FDLGRAEGYK NFCNKLWNAT RFVLMNTAGD TAHSPAQHQA GQDGQDVPRT PQPRTDAEQW
730 740 750 760 770 780
ILSRLAAVTA EAHAQFAAYR FDLLAQALYE FAWNEFCDWF VELAKPALNG DDTQAAASTR
790 800 810 820 830 840
HTLLYVLETL LRLLHPLIPF ITEELWCQVA PRLGIQATTL MLRPYPQPQQ LETTAFANAA
850 860 870 880 890 900
ADVEWLKIMV SALRRIRSTL NVPPSRRISL LLQGGQEVDR RRITHFAIAL HFLLKLEHID
910 920 930 940 950 960
WLSATTAAPP SATAIVGSLK LLVPLEGLID VDAERARLDK EIKRVESEID KSNGKLSNAV
970 980 990
FVQNAPTAVV EQERSRLREW TTQLNGLRER RTTL